A luminal flavoprotein in endoplasmic reticulum-associated degradation [PDF]
Proceedings of the National Academy of Sciences, 2009 The quality control system of the endoplasmic reticulum (ER) discriminates between native and nonnative proteins. The latter are degraded by the ER-associated degradation (ERAD) pathway. Whereas many cytosolic and membrane components of this system are known, only few luminal players have been identified.
Riemer, Jan +5 more
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Mechanism and components of endoplasmic reticulum-associated degradation [PDF]
Journal of Biochemistry, 2009 The folding of secretory and membrane proteins takes place in the endoplasmic reticulum (ER). The quality of the proteins folded in the ER is carefully monitored by an ER quality control mechanism that allows only correctly folded proteins to be transported to their final destination, and misfolded or unassembled proteins to be retained in the ER and ...
Jun, Hoseki +2 more
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Membrane-associated RING ubiquitin ligase RNF-121 and advancement of cancer [PDF]
Cellular, Molecular and Biomedical ReportsExploration of E3 ubiquitin ligases as potential therapeutic targets has been ongoing for two to three decades. Various chemicals and drugs have been developed to either upregulate or inhibit the activity of E3 ligases, aiming to mitigate several ...
Somesh Roy
doaj +1 more source
Specificity and Regulation of the Endoplasmic Reticulum‐Associated Degradation Machinery [PDF]
Traffic, 2013 The endoplasmic reticulum‐associated degradation (ERAD) machinery selects native and misfolded polypeptides for dislocation across the ER membrane and proteasomal degradation. Regulated degradation of native proteins is an important aspect of cell physiology. For example, it contributes to the control of lipid biosynthesis, calcium homeostasis and ERAD
Merulla Jessica +5 more
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Acta Veterinaria, 2023 The endoplasmic reticulum (ER) is crucial for the production, processing and transport of proteins. Infection with pathogens activates Unfolded Protein Response (UPR), which can lead to their survival/replication or elimination from the body.
Kholod Natalia +3 more
doaj +1 more source
Endoplasmic reticulum-associated degradation: a novel therapeutic avenue for ADPKD. [PDF]
Am J Physiol Cell PhysiolXu B, Staruschenko A.
europepmc +3 more sources
Cytosolic entry of Shiga-like toxin A chain from the yeast endoplasmic reticulum requires catalytically active Hrd1p [PDF]
, 2012 Background Escherichia coli Shiga-like toxin 1 normally traffics to the endoplasmic reticulum (ER) in sensitive mammalian cells from where the catalytic A chain (SLTxA1) dislocates to the cytosol to inactivate ribosomes.
Lynne M. Roberts (150050) +21 more
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Estrogens Promote Misfolded Proinsulin Degradation to Protect Insulin Production and Delay Diabetes
Cell Reports, 2018 Summary: Conjugated estrogens (CE) delay the onset of type 2 diabetes (T2D) in postmenopausal women, but the mechanism is unclear. In T2D, the endoplasmic reticulum (ER) fails to promote proinsulin folding and, in failing to do so, promotes ER stress and
Beibei Xu +12 more
doaj +1 more source
Cyclosporine A-sensitive, cyclophilin B-dependent endoplasmic reticulum-associated degradation. [PDF]
PLoS ONE, 2010 Peptidyl-prolyl cis/trans isomerases (PPIs) catalyze cis/trans isomerization of peptide bonds preceding proline residues. The involvement of PPI family members in protein refolding has been established in test tube experiments.
Riccardo Bernasconi +5 more
doaj +1 more source
Folding-competent and folding-defective forms of Ricin A chain have different fates following retrotranslocation from the endoplasmic reticulum [PDF]
, 2010 We report that a toxic polypeptide retaining the potential to refold upon dislocation from the endoplasmic reticulum (ER) to the cytosol (ricin A chain; RTA) and a misfolded version that cannot (termed RTAΔ), follow ER-associated degradation (ERAD ...
Ladds, Graham +26 more
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